› 2pv7

X-ray diffraction
2Å resolution

Crystal structure of chorismate mutase / prephenate dehydrogenase (tyrA) (1574749) from Haemophilus influenzae RD at 2.00 A resolution

Released:
DOI: 10.2210/pdb2pv7/pdb
PDB entry 2pv7 coloured by chain, front view.
PDB entry 2pv7 coloured by chain, side view.
PDB entry 2pv7 coloured by chain, top view.
Source organism: Haemophilus influenzae
Primary publication:
The structure of Haemophilus influenzae prephenate dehydrogenase suggests unique features of bifunctional TyrA enzymes.
Chiu HJ, Abdubek P, Astakhova T, Axelrod HL, Carlton D, Clayton T, Das D, Deller MC, Duan L, Feuerhelm J, Grant JC, Grzechnik A, Han GW, Jaroszewski L, Jin KK, Klock HE, Knuth MW, Kozbial P, Krishna SS, Kumar A, Marciano D, McMullan D, Miller MD, Morse AT, Nigoghossian E, Okach L, Reyes R, Tien HJ, Trame CB, van den Bedem H, Weekes D, Xu Q, Hodgson KO, Wooley J, Elsliger MA, Deacon AM, Godzik A, Lesley SA, Wilson IA
Acta Crystallogr Sect F Struct Biol Cryst Commun 66 1317-25 (2010)
PMID: 20944228

Function and Biology Details

Reactions catalysed: 
Prephenate + NAD(+) = 4-hydroxyphenylpyruvate + CO(2) + NADH
Chorismate = prephenate
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-155152 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
T-protein Chains: A, B
Molecule details ›
Chains: A, B
Length: 298 amino acids
Theoretical weight: 34.28 KDa
Source organism: Haemophilus influenzae
Expression system: Escherichia coli
UniProt:
  • Canonical: P43902 (Residues: 81-377; Coverage: 79%)
Gene names: HI_1290, tyrA
Sequence domains:
Structure domains:

Ligands and Environments


Cofactor: Ligand NAD 2 x NAD
1 bound ligand:
Ligand TYR 2 x TYR
1 modified residue:
Ligand MSE 16 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL11-1
Spacegroup: P41212
Unit cell:
a: 127.79Å b: 127.79Å c: 100.62Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.163 0.161 0.194
Expression system: Escherichia coli

Quick links

Citations

1 review citation

Insight into de-regulation of amino acid feedback inhibition: a focus on structure analysis method.
Naz et al. (2023)
5 other articles

5 mentions without citation

Decision-making in structure solution using Bayesian estimates of map quality: the PHENIX AutoSol wizard.
Terwilliger et al. (2009)
4 more